5FCLL_ARATH
ID 5FCLL_ARATH Reviewed; 354 AA.
AC Q9SRE0; Q8GW33;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase-like protein COG0212;
DE AltName: Full=Protein CLUSTERS OF ORTHOLOGOUS GROUP 212;
DE Flags: Precursor;
GN Name=COG0212; OrderedLocusNames=At1g76730; ORFNames=F28O16.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21538139; DOI=10.1007/s10142-011-0224-5;
RA Pribat A., Blaby I.K., Lara-Nunez A., Jeanguenin L., Fouquet R., Frelin O.,
RA Gregory J.F., Philmus B., Begley T.P., de Crecy-Lagard V., Hanson A.D.;
RT "A 5-formyltetrahydrofolate cycloligase paralog from all domains of life:
RT comparative genomic and experimental evidence for a cryptic role in thiamin
RT metabolism.";
RL Funct. Integr. Genomics 11:467-478(2011).
CC -!- FUNCTION: May be involved in thiamine metabolism. Does not possess 5-
CC formyltetrahydrofolate cyclo-ligase activity in vitro.
CC {ECO:0000269|PubMed:21538139}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21538139}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:21538139}.
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000305}.
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DR EMBL; AC010718; AAF04436.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35883.1; -; Genomic_DNA.
DR EMBL; AK119107; BAC43679.1; -; mRNA.
DR EMBL; BT024883; ABD85154.1; -; mRNA.
DR PIR; G96795; G96795.
DR RefSeq; NP_565139.1; NM_106323.4.
DR AlphaFoldDB; Q9SRE0; -.
DR STRING; 3702.AT1G76730.1; -.
DR PaxDb; Q9SRE0; -.
DR PRIDE; Q9SRE0; -.
DR ProteomicsDB; 244507; -.
DR EnsemblPlants; AT1G76730.1; AT1G76730.1; AT1G76730.
DR GeneID; 844007; -.
DR Gramene; AT1G76730.1; AT1G76730.1; AT1G76730.
DR KEGG; ath:AT1G76730; -.
DR Araport; AT1G76730; -.
DR TAIR; locus:2030111; AT1G76730.
DR eggNOG; KOG4410; Eukaryota.
DR HOGENOM; CLU_031500_0_0_1; -.
DR InParanoid; Q9SRE0; -.
DR OMA; KTVYMAV; -.
DR OrthoDB; 1137978at2759; -.
DR PhylomeDB; Q9SRE0; -.
DR PRO; PR:Q9SRE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRE0; baseline and differential.
DR Genevisible; Q9SRE0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10420; -; 1.
DR InterPro; IPR002698; FTHF_cligase.
DR InterPro; IPR024185; FTHF_cligase-like_sf.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR13017; PTHR13017; 1.
DR Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..354
FT /note="5-formyltetrahydrofolate cyclo-ligase-like protein
FT COG0212"
FT /id="PRO_0000428720"
FT REGION 330..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 235..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 89
FT /note="K -> R (in Ref. 3; BAC43679)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> Y (in Ref. 3; BAC43679)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="A -> V (in Ref. 3; BAC43679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39559 MW; A79E2448C25A3771 CRC64;
MIRLSPGFAI NPRFRSDSFV NSQKPPFLSV QIGSQRRNLS RIGSENGDGV AFDAVAYEAD
RLSLDAAAME DMAETAKKEL ESDPDSDPKA WKWVIRKKMW DLMEARNYAM SPRPVHHRIP
NFVGASAAAR KLAELDAFRM AMVVKVNPDS PQKQIRFLTL SGEKKLLTPQ PRLRTGFFSV
LESDLLKPET IMEACTSVGV AKYGRAIGLD EKIKVDLIVI GSVAVNPQTG ARLGKGEGFA
ELEYGMLRYM GAIDDSTPVV TTVHDCQLVD DIPLEKLAIH DVPVDIICTP TRVIFTNTPI
PKPQGIYWDK LSPEKLRQIR ILRELKNRLE KKTGRKLPTG PSEKLPPTAE RKRR
